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If the serine phoshorylated by Protein Kinase A (PKA) on phosphofructokinase-2 (PFK-2) were mutated to an aspartate, how might this affect gluconeogenesis in the liver? The rate of gluconeogenesis would increase, since PKA would phoshporylate an aspartate instead of a drine residue on PFK-2, which would activate the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be increase, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be unchanged, since PKA would be unable to inhibit the formation of fructose-2,6-bisphosphate through phosphorylation of PFK-2. The rate of gluconeogenesis would be diminished, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be diminished, since PKA would be unable to inhibit the formation of fructose-2.6-bisphosphate through phosphorylation of PFK-2.

If the serine phoshorylated by Protein Kinase A (PKA) on phosphofructokinase-2 (PFK-2) were mutated to an aspartate, how might this affect gluconeogenesis in the liver? The rate of gluconeogenesis would increase, since PKA would phoshporylate an aspartate instead of a drine residue on PFK-2, which would activate the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be increase, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be unchanged, since PKA would be unable to inhibit the formation of fructose-2,6-bisphosphate through phosphorylation of PFK-2. The rate of gluconeogenesis would be diminished, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be diminished, since PKA would be unable to inhibit the formation of fructose-2.6-bisphosphate through phosphorylation of PFK-2.

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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If the serine phoshorylated by Protein Kinase A (PKA) on phosphofructokinase-2 (PFK-2) were mutated to an aspartate, how might this affect gluconeogenesis in the liver? The rate of gluconeogenesis would increase, since PKA would phoshporylate an aspartate instead of a drine residue on PFK-2, which would activate the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be increase, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be unchanged, since PKA would be unable to inhibit the formation of fructose-2,6-bisphosphate through phosphorylation of PFK-2. The rate of gluconeogenesis would be diminished, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be diminished, since PKA would be unable to inhibit the formation of fructose-2.6-bisphosphate through phosphorylation of PFK-2.
Transcribed Image Text:If the serine phoshorylated by Protein Kinase A (PKA) on phosphofructokinase-2 (PFK-2) were mutated to an aspartate, how might this affect gluconeogenesis in the liver? The rate of gluconeogenesis would increase, since PKA would phoshporylate an aspartate instead of a drine residue on PFK-2, which would activate the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be increase, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be unchanged, since PKA would be unable to inhibit the formation of fructose-2,6-bisphosphate through phosphorylation of PFK-2. The rate of gluconeogenesis would be diminished, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be diminished, since PKA would be unable to inhibit the formation of fructose-2.6-bisphosphate through phosphorylation of PFK-2.
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